Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 24, pp 3014–3038

GTPase activating proteins: structural and functional insights 18 years after discovery

Review

DOI: 10.1007/s00018-005-5136-x

Cite this article as:
Scheffzek, K. & Ahmadian, M.R. Cell. Mol. Life Sci. (2005) 62: 3014. doi:10.1007/s00018-005-5136-x

Abstract.

The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) by guanine nucleotide binding proteins (GNBPs) is a fundamental process in living cells and represents an important timer in intracellular signalling and transport processes. While the rate of GNBP-mediated GTP hydrolysis is intrinsically slow, direct interaction with GTPase activating proteins (GAPs) accelerates the reaction by up to five orders of magnitude in vitro. Eighteen years after the discovery of the first GAP, biochemical and structural research has been accumulating evidence that GAPs employ a much wider spectrum of chemical mechanisms than had originally been assumed, in order to regulate the chemical players on the catalytic protein-protein interaction stage.

Key words.

Signal transduction cancer GTPase cycle arginine finger switch region cytoskeleton nuclear transport protein targeting 

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Structural and Computational Biology Programme and Developmental Biology ProgrammeEuropean Molecular Biology LaboratoryHeidelbergGermany
  2. 2.Department of Structural BiologyMax-Planck-Institute of Molecular PhysiologyDortmundGermany

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